Recombinant Rat Hemopexin Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-2386

Recombinant Rat Hemopexin Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-2386
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Product Overview

Tag His
Host Species Rat
Accession P20059
Description A DNA sequence encoding the rat Hpx (P20059.3) (Met1-Gln460) was expressed with a His tag at the C-terminus.
Source HEK293
Predicted N Terminal Asn 24
AA Sequence Met1-Gln460
Molecular Weight The recombinant rat Hpx consists 448 a.a. and predicts a molecular mass of 50.4 kDa.
Purity >90% as determined by SDS-PAGE
Endotoxin < 1.0 EU per μg protein as determined by the LAL method.
Bioactivity Please contact us for detailed information
Formulation Lyophilized from sterile PBS, pH 7.4..
Stability The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage For Research Use Only
Storage Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function Binds heme and transports it to the liver for breakdown and iron recovery, after which the free hemopexin returns to the circulation.
Subcellular Location Secreted.
Protein Families Hemopexin family
Database References
Tissue Specificity Expressed by the liver and secreted in plasma.

Gene Functions References

  1. Data suggest that apo-hemopexin isolated from plasma exchibits low endogenous levels of tyrosine nitration in the peptide YYCFQGNQFLR in the heme-binding site of human hemopexin, which was similarly nitrated in rabbit and rat hemopexins; heme binding by hemopexin declined as tyrosine nitration proceeded in vitro. PMID: 28596380
  2. Hemopexin was identified as upregulated protein in the small intestine exposed to indomethacin. PMID: 22486875
  3. hemopexin mRNA was low or undetectable in livers of hypophysectomized rats, however, daily treatment with bovine growth hormone for 10 days restored hemopexin mRNA levels PMID: 12850285
  4. intracellular calcium and protein kinase C activation are involved in the regulation of Hpx. PMID: 12850286

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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